The type II fatty acid synthase pathway of Plasmodium falciparum is a validated unique target for developing novel antimalarials because of its intrinsic differences from the type I pathway operating in humans. beta-Ketoacyl-acyl carrier protein reductase is the only enzyme of this pathway that has no isoforms and thus selective inhibitors can be developed for this player of the pathway. We rep...

Cerulenin, [(2S,3R)-2,3-epoxy-4-oxo-7,10-dodecadienoylamide], a mycotoxin produced by Cephalosporium caerulens, irreversibly inactivated 6-methylsalicylic acid synthase from Penicillium patulum. A combination of radiolabelling studies with [3H]cerulenin, proteolytic and chemical digestion and N-terminal sequencing of labelled peptides indicated that the site of cerulenin modification is the hig...

Two classes of Escherichia coli unsaturated fatty acid auxotrophs, which are complementary both in vivo and in vitro, have been utilized to study unsaturated fatty acid synthesis. /3 Hydroxydecanoyl thioester dehydrase, which catalyzes the first committed reaction in the unsaturated fatty acid synthetic pathway, is defective in one class, fab A. The defect in the second class, fab B, was unknow...

Anthocyanins, Flavonoids, Chalcone Synthase, Genetic Control, Matthiola incana Chalcone synthase activity was demonstrated in enzyme preparations from flowers of defined genotypes of Matthiola incana (stock). The product formed from 4-coumaroyl-CoA and malonylCoA was naringenin and not the isomeric chalcone, because chalcone isomerase was also present in the reaction mixture. Chalcone synthase ...

Acetoacetyl-CoA is the precursor of 3-hydroxy-3-methylglutaryl (HMG)-CoA in the mevalonate pathway, which is essential for terpenoid backbone biosynthesis. Acetoacetyl-CoA is also the precursor of poly-beta-hydroxybutyrate, a polymer belonging to the polyester class produced by microorganisms. The de novo synthesis of acetoacetyl-CoA is usually catalyzed by acetoacetyl-CoA thiolase via a thioes...

The Streptomyces coelicolor fab (fatty acid biosynthesis) gene cluster (fabD-fabH-acpP-fabF) is cotranscribed to produce a leaderless mRNA transcript. One of these genes, fabH, encodes a ketoacyl synthase III that is essential to and is proposed to be responsible for initiation of fatty acid biosynthesis in S. coelicolor.

We use mass spectrometry analysis and molecular modelling to show the established antimicrobial inhibitor 4,5-dichloro-1,2-dithiol-3-one (HR45) acts by forming a covalent adduct with the target β-ketoacyl-ACP synthase III (FabH). The 5-chloro substituent directs attack of the essential active site thiol (C112) via a Michael-type addition elimination reaction mechanism.